| Author | Search for: Bateman, K.; Search for: Thibault, P.; Search for: Yang, K.; Search for: White, R.; Search for: Vining, L. |
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| Format | Text, Article |
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| Subject | streptogramin; antibiotic resistance; enzyme; substrate specificity; Streptomyces lividans |
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| Abstract | LC–MS and LC–MS/MS analyses indicated that an enzyme responsible for inactivating the antibiotic etamycin is specific for streptogramins and acts on both type B‐I and B‐II streptogramin subgroups. No enzymatic activity was detected for other cyclodepsipeptides such as surfactins and viscosin. It was demonstrated using analogs of etamycin that the picolinyl moiety is essential to obtain enzyme‐generated ring‐opened compounds. Because the picolinyl moiety is also essential for the biological activity of streptogramins, it is proposed that this residue is a distinctive topographic feature in the binding of this group of antibiotics to enzyme active sites. |
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| Publication date | 1997-11 |
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| Publisher | Wiley |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NRC number | BATEMAN1997A |
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| NPARC number | 9376073 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | bf3f15d5-718b-4ef3-9c1f-c572f41d81c7 |
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| Record created | 2009-07-10 |
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| Record modified | 2020-03-20 |
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